Isothermal titration calorimetry measures heat accompanying additions of one binding partner to another at controlled temperature. With suitable concentration ranges, stoichiometry and a binding model, it can estimate affinity and binding enthalpy; dilution and buffer effects need controls.
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Isothermal titration calorimetry (ITC) is a sensitive and versatile technique used to measure the thermodynamics of molecular interactions, such as binding affinities, reaction kinetics, and the enthalpic and entropic changes associated with these processes. It provides real-time, quantitative data on the heat change that occurs during a chemical reaction or physical interaction, typically between a ligand and a macromolecule (like a protein, nucleic acid, or polymer).